Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.

The whole of the physical, chemical, and biochemical processes carried out by multicellular organisms to break down ingested nutrients into components that may be easily absorbed and directed into metabolism.

Keywords

Protein involved in the process whereby nutrients are rendered soluble and capable of being absorbed by the organism or cell, by action of various hydrolytic enzymes that break down proteins, carbohydrates, fats, etc.

Proteolytic enzyme with an aspartate residue (Asp) in its active site. There are many families of aspartyl proteases. The most well known one is the pepsin family (A1 in MEROPS classification) which is known to exist in vertebrates, fungi, plants, retroviruses and some plant viruses.

Protein which is part of a reference proteome. Reference proteomes are a subset of proteomes that have been selected either manually or algorithmically according to a number of criteria to provide a broad coverage of the tree of life and a representative cross-section of the taxonomic diversity found within UniProtKB, as well as the proteomes of well-studied model organisms and other species of interest for biomedical research.